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Database: UniProt
Entry: D3V9V9_XENNA
LinkDB: D3V9V9_XENNA
Original site: D3V9V9_XENNA 
ID   D3V9V9_XENNA            Unreviewed;       384 AA.
AC   D3V9V9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 47.
DE   SubName: Full=Bifunctional: chorismate mutase P (N-terminal) prephenate dehydratase (C-terminal) {ECO:0000313|EMBL:CBJ89347.1};
DE            EC=4.2.1.51 {ECO:0000313|EMBL:CBJ89347.1};
DE            EC=5.4.99.5 {ECO:0000313|EMBL:CBJ89347.1};
GN   Name=pheA {ECO:0000313|EMBL:CBJ89347.1};
GN   OrderedLocusNames=XNC1_1276 {ECO:0000313|EMBL:CBJ89347.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ89347.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ89347.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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DR   EMBL; FN667742; CBJ89347.1; -; Genomic_DNA.
DR   RefSeq; WP_010845352.1; NC_014228.1.
DR   STRING; 406817.XNC1_1276; -.
DR   EnsemblBacteria; CBJ89347; CBJ89347; XNC1_1276.
DR   KEGG; xne:XNC1_1276; -.
DR   eggNOG; ENOG4105CQC; Bacteria.
DR   eggNOG; COG0077; LUCA.
DR   eggNOG; COG1605; LUCA.
DR   HOGENOM; HOG000018972; -.
DR   KO; K14170; -.
DR   OMA; REVMSAC; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR   GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.59.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR   InterPro; IPR036263; Chorismate_II_sf.
DR   InterPro; IPR036979; CM_dom_sf.
DR   InterPro; IPR002701; CM_II_prokaryot.
DR   InterPro; IPR010952; CM_P_1.
DR   InterPro; IPR001086; Preph_deHydtase.
DR   InterPro; IPR018528; Preph_deHydtase_CS.
DR   Pfam; PF01817; CM_2; 1.
DR   Pfam; PF00800; PDT; 1.
DR   PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR   SMART; SM00830; CM_2; 1.
DR   SUPFAM; SSF48600; SSF48600; 1.
DR   TIGRFAMs; TIGR01797; CM_P_1; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR   PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Isomerase {ECO:0000313|EMBL:CBJ89347.1};
KW   Lyase {ECO:0000313|EMBL:CBJ89347.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN        1     90       Chorismate mutase. {ECO:0000259|PROSITE:
FT                                PS51168}.
FT   DOMAIN      103    283       Prephenate dehydratase.
FT                                {ECO:0000259|PROSITE:PS51171}.
FT   DOMAIN      297    374       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   COILED        5     25       {ECO:0000256|SAM:Coils}.
FT   BINDING       9      9       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      26     26       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      37     37       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      46     46       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      50     50       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      82     82       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   BINDING      86     86       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001500-1}.
FT   SITE        276    276       Essential for prephenate dehydratase
FT                                activity. {ECO:0000256|PIRSR:PIRSR001500-
FT                                2}.
SQ   SEQUENCE   384 AA;  43544 MW;  87582887210F2202 CRC64;
     MEQNLVNLRE KISNIDADLL DLLAKRRQLA NNIAKTKLLE NRPIRDKNRE RELLNVLITK
     GKNRGLDGFY ITRLFQMIIE DSVLTQQALL QQHLNQTHFD SARITFLGPK GSYSHLAARQ
     FAARHFNQLV ECSCQKFSDI FSLIEIGQAD YGILPLENTS SGAINEVYDL LQHTPLSIVG
     EITLPINHCL LVTEYTDISR IKTVYSHSQP FQQCSQYLNK HPHWNIIYCE STADAMQKVA
     ELNSPEVAAL GSEAGGALYG LRVLENNLAN QQENSTRFIV VARKPIEVSE QVPSKTTFIM
     STGQQSGALV DTLIILKKHN IIMRKLESRP INGKPWEEMF YIDVQANLRS IKMQQALKEL
     TEITRFLKVL GCYPSENVVP IDPI
//
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